Regeneration of the photoprotein aequorin

  title={Regeneration of the photoprotein aequorin},
  author={O. Shimomura and F. Johnson},
THE photoprotein aequorin (molecular weight about 30,000) isolated from the bioluminescent jellyfish Aequorea aequorea1–3 emits blue light (λm a x 470 nm)4 by an intramolecular reaction in aqueous solution when Ca2+ is added, in the presence or absence of molecular oxygen1. This reaction has been postulated5 to follow the scheme in (Fig. 1), in which an essential component H2O2 of aequorin is bound to the protein part in a form such as a peroxyacid or an α-hydroxyhydroperoxide which readily… Expand
The crystal structure of the photoprotein aequorin at 2.3 Å resolution
The structure of recombinant aequorin is found to be a globular molecule containing a hydrophobic core cavity that accommodates the ligand coelenterazine-2-hydroperoxide and suggests a mechanism by which calcium activation may occur. Expand
Uses and Physicochemical Properties of the Photoprotein Aequorin
The calcium-sensitive bioluminescent photoprotein aequorin is proving to be a useful tool for the measurement of [Ca2+] in living cells. Use of this protein has distinct advantages over otherExpand
Comparisons of the coding regions of the two cDNAs show there are 52 nucleotide differences, 19 of which are responsible for 18 amino acid replacements, which explain the microheterogeneity observed at 17 positions during the sequencing of native apoaequorin. Expand
[30] Introduction to the bioluminescence of medusae, with special reference to the photoprotein aequorin
This chapter discusses the bioluminescence of Medusae, with special reference to the photoprotein aequorin, which must be considered to represent an enzyme intermediate, as hypothetically suggested by several investigators. Expand
Amino acid sequence of the calcium-dependent photoprotein aequorin.
It is demonstrated that aequorin is a member of the Ca(II) binding protein superfamily and possesses three internally homologous domains which were judged to be EF-hand Ca( II) binding domains by several different criteria. Expand
The discovery of aequorin and green fluorescent protein
In the characterization of these proteins, information obtained from the bioluminescence of the ostracod Cypridina played an extremely important role, and without the information gained on CyPRidina luminescence, the characterize of aequorin would not have been possible. Expand
Selective protein modification by the hydroperoxide intermediate in a photoprotein, aequorin.
During the course of protein modification program, a recombinant aequorin was employed, the apo-protein reconstituted with coelenterazine, and it was found that the photolytic hyperperoxide modified three -S-SCH2CHOHCHOH CHOHCH2SH groups to -S(=O)OH of terminal DTT connected to cysteine residues of the C145, C152 and C180. Expand
Photoprotein aequorin: use as a reporter enzyme in studying gene expression in mammalian cells.
It is reported here that aequorin can be used as a reporter enzyme to monitor gene expression in eukaryotic cells and was shown to be as sensitive as the conventional CAT assay. Expand
Oxidation of a cyclic tripeptide by molecular oxygen and the development of fluorescence in the Aequorea green fluorescent protein
Abstract The jellyfish, Aequorea victoria , emits a greenish light from photocytes located along the margin of its umbrella. The source of the light is a green fluorescent protein (GFP) within theExpand
The crystal structures of semi‐synthetic aequorins
The differences of various semi‐synthetic aequorins in Ca2+‐sensitivity and reaction rate are explained by the capability of the involved groups and structures to undergo conformational changes in response to the Ca2+, particularly in the coelenterazine moiety. Expand


Calcium Binding, Quantum Yield, and Emitting Molecule in Aequorin Bioluminescence
The extreme sensitivity to Ca2+, much more than to Sr2+, provides a basis for quick microdetermination of Ca2+ in biological fluids and has been used in detecting the relation ofCa2+ to contraction of single muscle fibres and to activity of mitochondria. Expand
Preparation and use of aequorin for rapid microdetermination of Ca 2+ in biological systems.
The photoprotein aequorin extracted from the luminescent jellyfish Aequorea aequorea offers unique advantages for detecting the presence or changes in concentration of Ca2+ in biological systems and for investigating the action of poisons such as cyanide, tetrodotoxin and so on, on biological processes12–14. Expand
Intermolecular energy transfer in the bioluminescent system of Aequorea.
In the present study, GFP has been purified, crystallized, and partially characterized and an energy transfer in citro from aequorin to this protein has been demonstrated. Expand
Chemical nature of bioluminescence systems in coelenterates.
  • O. Shimomura, F. Johnson
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1975
Analysis of substances involved in light-emitting reactions among bioluminescent coelenterates has revealed a pronounced uniformity in the structural features of initial reactants, i.e., "luciferins"Expand
Renilla luciferin as the substrate for calcium induced photoprotein bioluminescence. Assignment of luciferin tautomers in aequorin and mnemiopsin.
The study of the effects of pH and protic and aprotic solvents on the spectral properties of Renilla (sea pansy) luciferin and a number of its analogs suggests that the native chromophore in both photoproteins is RenillaLuciferin (or a nearly identical derivative). Expand
The "energized state" of mitochondria: lifetime and ATP equivalence.
The endogenous mitochondrial Ca2+ has been found to be in a highly dynamic state, and the proton movements observed on activation of respiration can be considered not primary, but associated with ion movements. Expand
Evidence for similar biochemical requirements for bioluminescence among the coelenterates
We present evidence that the chemical requirements among all the bioluminescent coelenterates that have been examined are very similar or identical to those already described for Renilla by CormierExpand
2-(p-Hydroxybenzyl)-6-(p-hydroxyphenyl)-3,7-dihydroimidazo[1,2-a]pyrazin-3-one was isolated from the squid, Watasenia scintillans. Its structure was determined by synthesis. It is considered to be aExpand
Calcium influx in active Aplysia neurones detected by injected aequorin.
ACTION potentials may be recorded in Aplysia1,2 and Helix3 neurones in sodium and in calcium-free solutions, provided that either ion is present in the medium. The inward current may be due to both,Expand
Calcium Transient in Presynaptic Terminal of Auid Giant Synapse: Detection with Aequorin
Microinjection of aequorin, a bioluminescent protein sensitive tocalcium, into the presynaptic terminal of the squid giant synapse demnonstrated an increase in intracellular calcium ion concentrationExpand